Hrp labeled goat anti rabbit igg

Manufactured by Beyotime

Sourced in China, United States

HRP-labeled goat anti-rabbit IgG is a secondary antibody conjugated with horseradish peroxidase (HRP). It is designed to bind to and detect rabbit primary antibodies in various immunoassay applications.

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Lab products found in correlation

Hrp labeled goat anti mouse igg, by Beyotime (30 mentions) Ripa lysis buffer, by Beyotime (6 mentions) Hrp labeled donkey anti goat igg, by Beyotime (4 mentions) Gapdh, by Cell Signaling Technology (4 mentions) Bca protein assay kit, by Beyotime (4 mentions) Pvdf membrane, by Merck Group (4 mentions) Horseradish peroxidase hrp labeled goat anti mouse igg, by Beyotime (3 mentions) Gapdh, by Proteintech (3 mentions) Beyoecl plus, by Beyotime (3 mentions) A0216, by Beyotime (3 mentions) A0208, by Beyotime (3 mentions) Surepage gel, by GenScript (3 mentions) Penicillin streptomycin, by Thermo Fisher Scientific (2 mentions) E cadherin, by Cell Signaling Technology (2 mentions) Rabbit anti human cd9 antibody, by Proteintech (2 mentions) Rabbit anti human tsg101 antibody, by Proteintech (2 mentions) Bca kit, by Beyotime (2 mentions) Quantity one software, by Bio-Rad (2 mentions) Anti gapdh, by Cell Signaling Technology (2 mentions) Enhanced chemiluminescent reagent, by Beyotime (2 mentions)

Close spelling variants of this product

HRP-labeled goat anti-rabbit Goat anti-rabbit HRP

67 protocols using hrp labeled goat anti rabbit igg

miR-15a Regulates NSCLC Proliferation via Smad3

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Annexin V-FITC, MTT kits, and HRP-labeled Goat Anti-Rabbit IgG (A0208) were from Beyotime Biotechnology; RPMI-1640 medium, fetal bovine serum, penicillin-streptomycin and trypsin from Gibco; Thermo Fisher Scientific, Inc.; TRIzol reagent and Transwell cell culture plates from Corning Inc.; Promega M-MLV reverse transcription kits from Promega Corporation; YBR Premix Ex Taq from Takara Biotechnology Co., Ltd.; miR-15a overexpression plasmid was synthesized by Guangzhou RiboBio Co., Ltd.; Lipofectamine^® 3000 Transfection kit was from Invitrogen; Thermo Fisher Scientific, Inc.; Smad3 protein (rabbit anti-human Smad3 monoclonal antibody, ab40854) from Abcam; GAPDH antibody (mouse anti-human GAPDH monoclonal antibody, SC-32233) from Santa Cruz Biotechnology, Inc.; Immobilon Western HRP from Thermo Fisher Scientific, Inc.
Human NSCLC cell lines (A549, H1299, and H1975) and the normal lung cells (BEAS-2B) were all from Shanghai Institute of Biochemistry and Cell Biology, CAS. The cells were cultured in DMEM (Corning Inc.) medium containing 10% fetal bovine serum (FBS) (Thermo Fisher Scientific, Inc.) and 1% streptomycin (Corning Inc.) at 37°C with the concentration of 5% CO₂.

Guo S., Li M., Li J, & Lv Y. (2019). Inhibition mechanism of lung cancer cell metastasis through targeted regulation of Smad3 by miR-15a. Oncology Letters, 19(2), 1516-1522.

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Western Blot Analysis of Spinal Cord Proteins

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The spinal cord tissues (L3-L4) were homogenized in a lysis buffer containing Protease Inhibitor Cocktail (p8340, Sigma-Aldrich) [19 (link)]. The protein concentration was confirmed with BCA protein concentration determination assay kit (P0010, Beyotime, Shanghai, China). The protein samples were separated by SDS-PAGE gels and transferred onto polyvinylidene fluoride membrane (IPVH00010, Millipore). The membrane was sealed with 5% skim milk for 2 h at room temperature, subsequently incubated at 4°C overnight with the primary antibodies: Mtf1 (1 : 500; Santa Cruz Biotechnology, CA, USA), p-ERK1/2 (1 : 5000; Sigma), ERK1/2 (1 : 1000; Santa Cruz Biotechnology), GFAP (1 : 1000; Cell Signaling Technology, Danvers, MA, USA) and β-actin (1 : 2000; Santa Cruz Biotechnology). The membrane was washed for 5 min/time 3 times at room temperature, incubated for 2 h in the corresponding secondary antibody: HRP-labeled goat anti-mouse IgG (1 : 1000; Beyotime), HRP-labeled goat anti-rabbit IgG (1 : 1000; Beyotime) and HRP-labeled donkey anti-goat IgG (1 : 1000; Beyotime) at room temperature. The membrane was then washed for 5 min/time 6 times, the immune complexes were detected by ECL chemiluminescent assay kit (Biosharp, Guangzhou, China). Signal intensity of band analyses was conducted with ImageJ software (Alliance Q9).

Hao L.Y., Zhang M., Tao Y., Xu H., Liu Q., Yang K., Wei R., Zhou H., Jin T., Liu X.D., Xue Z., Shen W., Cao J.L, & Pan Z. (2022). miRNA-22 Upregulates Mtf1 in Dorsal Horn Neurons and Is Essential for Inflammatory Pain. Oxidative Medicine and Cellular Longevity, 2022, 8622388.

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Western Blot Analysis of Protein Expression

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Samples were treated with RIPA Lysis Buffer (Solarbio, Beijing, China) to extract the total protein. The proteins were quantified and stored at −20°C before use. We prepared 10% sodium dodecyl sulfate polyacrylamide gel to isolate the proteins. After transfer to nitrocellulose membrane, the bands were blocked with 5% non-fat milk. Then, the corresponding primary antibodies and secondary antibodies were diluted to appropriate concentrations and added to the protein bands, respectively. Finally, the protein bands were scanned with Tanon 5200 (Tanon, Shanghai, China). Integrated density value was used to calculate the relative protein quantity. The antibodies and reagents used were: ARHGAP24 (Abcam, ab203874, 1: 500); MMP9 (Abcam, ab76003, 1: 1000); VEGF (Abcam, ab69479, 1: 1000); Vimentin (Cell Signaling Technology, #5471, 1: 1000); E-cadherin (Cell Signaling Technology, #14472, 1: 1000); β-catenin (Abcam, ab32572, 1: 5000); GAPDH (Cell Signaling Technology, #5174, 1: 2000); HRP-labeled Goat Anti-Rabbit IgG (Beyotime, A0208, 1: 1000); HRP-labeled Donkey Anti-Goat IgG (Beyotime, A0181, 1: 1000); HRP-labeled Goat Anti-Mouse IgG (Beyotime, A0216, 1: 1000).

Wang L., Shen S., Wang M., Ding F., Xiao H., Li G, & Hu F. (2019). Rho GTPase Activating Protein 24 (ARHGAP24) Silencing Promotes Lung Cancer Cell Migration and Invasion by Activating β-Catenin Signaling. Medical Science Monitor : International Medical Journal of Experimental and Clinical Research, 25, 21-31.

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Western Blot Analysis of Apoptosis-Related Proteins

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The lung tissues of mice were pooled together and lysed using RIPA lysis buffer (Beyotime Biotech, Shanghai, China) to obtain the proteins, which were then quantified, loaded onto SDS-PAGE gels, and electro-transferred onto PVDF membranes (Amersham Biosciences, Piscataway, NJ, USA). PVDF membranes were blocked with 5% non-fat milk and then incubated with rabbit anti-human Bcl-XL (Cat. No. ab32370, 1: 3000), rabbit anti-human Bcl-2 (Cat. No. ab32124, 1: 3000), rabbit anti-human Bak (Cat. No. ab32371, 1: 2000), rabbit anti-human Bax (Cat. No. ab182733, 1: 2000), rabbit anti-human RanBPM (Cat. No. ab205954, 1: 2000), rabbit anti-cleaved caspase-3 (Cat. No. ab2302, 1: 2000), and rabbit anti-human β-actin (Cat. No. ab1376, 1: 2000) overnight at 4°C. Subsequently, PVDF membranes were washed in phosphate-buffered saline Tween-20 (PBST, Beyotime Biotech) and incubated using HRP-labeled goat anti-rabbit IgG (Cat. No. ab6721, 1: 1000) for 2 h at room temperature. Western blotting bands were visualized with a BeyoECL kit (Cat. No. P0018S, Beyotime Biotech). Finally, stained images were analyzed with the Tanon 5200 Automatic Chemiluminescence Imaging Analysis System (Tanon Sci. Tech. Co., Shanghai, China).

Lv X., Lu X., Zhu J, & Wang Q. (2020). Lipopolysaccharide-Induced Acute Lung Injury Is Associated with Increased Ran-Binding Protein in Microtubule-Organizing Center (RanBPM) Molecule Expression and Mitochondria-Mediated Apoptosis Signaling Pathway in a Mouse Model. Medical Science Monitor : International Medical Journal of Experimental and Clinical Research, 26, e923172-1-e923172-8.

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Exosome Protein Characterization Protocol

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The protein in U-EXO was collected using RIPA lysing buffer (Beyotime, China). Protein concentration was determined using a BCA kit (Beyotime, China). The CD9 and TSG101 protein expression in U-EXO were determined by western blot. Rabbit anti-human CD9 antibody (PROTEINTECH, USA) and rabbit anti-human TSG101 antibody (PROTEINTECH, USA) were used. HRP-labeled Goat Anti-rabbit IgG (Beyotime, China) was used as the secondary antibody.

Cao Y., Shi Y., Yang Y., Wu Z., Peng N., Xiao J., Dou F., Xu J., Pei W., Fu C., Chen P, & Wang Y. (2022). Urinary exosomes derived circRNAs as biomarkers for chronic renal fibrosis. Annals of Medicine, 54(1), 1966-1976.

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Western Blot Analysis of Protein Targets

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Equal amounts of protein (20–30 μg) were separated by 10% SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to a polyvinylidene fluoride membrane (PVDF, Millipore, Billerica, MA, USA). The membrane was blocked for 1 h with 5% fat-free dried milk at RT, then incubated with primary antibodies (Santa Cruz Biotechnology) against A3AR (1:800 dilution), NF-κB p65 (1:600 dilution), IκB-α (1:400 dilution), p-IκB-α (1:400 dilution), Tubulin (1:1,000 dilution), or β-actin (1:1,000 dilution) at 4°C overnight. Membranes were washed three times with Tris-buffered saline with Tween-20 (TBS-T) and incubated with the corresponding secondary antibodies (HRP-labeled Goat Anti-mouse IgG, HRP-labeled Goat Anti-rabbit IgG, HRP-labeled Donkey Anti-goat IgG; 1:1,000; Beyotime, China) for 1 h at room temperature. Signals were detected with an electrochemiluminescence (ECL) detection reagent (Beyotime, China). The images were obtained on Kodak film and quantified by Quantity One software (Bio-Rad, Hercules, CA, USA).

Ren T., Tian T., Feng X., Ye S., Wang H., Wu W., Qiu Y., Yu C., He Y., Zeng J., Cen J, & Zhou Y. (2015). An adenosine A3 receptor agonist inhibits DSS-induced colitis in mice through modulation of the NF-κB signaling pathway. Scientific Reports, 5, 9047.

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Gastric Cancer Drug Resistance Model

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The human gastric cancer cell line BGC823 was purchased from KeyGEN BioTECH Co., Ltd. (China).
The drug-resistant cell line BGC823/5-Fu was established by the low-dose multiple shock method in our previous research [17 (link)] and stored at -196 °C. The drug resistance index of BGC823/5-Fu was 13.
The serum-free medium (SFM) was composed of 95% DMEM/F12 (Gibco, USA), 1% 2 µg/ml EGF (Peprotech, USA), 1% 2 µg/ml bFGF (Peprotech, USA), 2% B27 (Gibco, USA), 1% 100 U/ml penicillin/streptomycin (Gibco, USA) and 0.4 U insulin (Sigma, USA). The IGF-1 was purchased from Sigma (USA). The P-gp, MRP1, PI3K, p-PI3K, AKT, p-AKT, Nrf2 and β-actin antibodies were purchased from Bioss, Inc. (China) and Proteintech Group, Inc. (USA). HRP-labeled Goat Anti-Rabbit IgG, HRP-labeled Goat Anti-Mouse IgG and Alexa Fluor 488-labeled Goat Anti-Rabbit IgG were purchased from Beyotime Biotechnology (China). The Annexin V-FITC/PI Kit was purchased from KeyGEN BioTECH Co., Ltd. (China). CD44 MicroBead Kit was purchased from Miltenyi Biontec. (Germany). Lipofectamine2000 was purchased from Invitrogen (USA).

Huang W., Wen F., Gu P., Liu J., Xia Y., Li Y., Zhou J., Song S., Ruan S., Gu S., Chen X, & Shu P. (2022). The inhibitory effect and mechanism of Yi-qi-hua-yu-jie-du decoction on the drug resistance of gastric cancer stem cells based on ABC transporters. Chinese Medicine, 17, 93.

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Extraction and Characterization of Mori Cortex Bioactive Compounds

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The raw medicinal herb Mori cortex was obtained from the Shanghai Yan-He-Tang Traditional Chinese Medicine Company. The raw herb was botanically authenticated by Prof Yiming Li in the School of Pharmacy, Shanghai University of Traditional Chinese Medicine (Shanghai, China). The voucher specimen (No. MC001) was deposited at the Herbarium of the Department of TCM Chemistry, School of Pharmacy, Shanghai University of Traditional Chinese Medicine. MC was extracted separately using the following process: one kilogram of Mori cortex was reflux extracted with five kilograms of 70% alcohol twice, 90 min each time. The extract solution was allowed to stand overnight, then filtered. The filtrate was concentrated to a small volume under reduced-pressure evaporation and dried by lyophilization. The extract yield after freeze drying was 11.6% and was named MCE. STZ was purchased from Sigma-Aldrich Chemicals Pvt Ltd (USA). All primary antibodies were from Abcam (UK) except for the β-actin primary antibody, which was from Biosynthesis Biotechnology CO, LTD (China). Secondary antibodies were HRP-labeled Goat Anti-Rabbit IgG from Beyotime (China). All other chemicals used were of analytical grade.

Ma L., Ni H., Zou X., Yuan Y., Luo C., Liu B., Wang F., Xi Y., Chu Y., Xu P., Qiu X., Li S, & Bu S. (2017). Mori cortex prevents kidney damage through inhibiting expression of inflammatory factors in the glomerulus in streptozocin-induced diabetic rats. Iranian Journal of Basic Medical Sciences, 20(6), 715-721.

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Protein Expression Analysis in Hippocampus and Cortex

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Western blot analysis was performed as previously reported (Liu et al., 2015 (link); Li et al., 2015 (link)). Three mice from each group were sacrificed after WMW test, and the hippocampal and cortical tissues were collected and homogenized in RIPA lysis buffer (1:5, w/v). Protein concentrations were determined by BCA protein assay kit. An aliquot of 45 µg of protein was applied for electrophoresis followed by the transferring of protein to the polyvinylidene difluoride (PVDF) membranes. The membranes were blocked with 5% nonfat dry milk in TBST buffer for one hour at room temperature, and incubated with the primary antibody: anti-CNTF (1:1,000), BDNF (1:1,000), and GDNF (1:1,000) at 4 °C overnight. Next, HRP-labeled goat anti-rabbit IgG (Beyotime Biotechnology, Jiangsu, China; A0208, 1:2,000) was incubated with the membrane at room temperature for one hour. The blots were visualized using the enhanced ECL Western blot detection kit (7Sea Biotech, Shanghai, China) and scanned to Gel Imaging. The band intensity was quantified using Quantity One 1-D analysis software v4.52 (BioRad, Hercules, California, USA).

Nie J., Tian Y., Zhang Y., Lu Y.L., Li L.S, & Shi J.S. (2016). Dendrobium alkaloids prevent Aβ25–35-induced neuronal and synaptic loss via promoting neurotrophic factors expression in mice. PeerJ, 4, e2739.

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Western Blotting for Protein Analysis

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Western blotting was performed as previously described (Gong et al., 2013 (link)). The primary antibodies used were as follows: anti-p38 MAPK (Cell Signaling Technology, 1:1000); anti-phospho-p38 MAPK (Cell Signaling Technology, 1:1000); anti-GAPDH (Cell Signaling Technology, 1: 1000); anti-Bcl-2 (Affinity Biosciences, 1: 1000); anti-Bax (Cell Signaling Technology, 1: 1000); anti-β-actin (Cell Signaling Technology, 1: 1000); anti-p53 (Cell Signaling Technology, 1: 1000); anti-phosphor-p53 (Affinity Biosciences, 1: 1000); HRP-labeled goat anti-rabbit IgG (Beyotime Biotechnology, 1: 1000), and HRP-labeled goat anti-mouse IgG (Beyotime Biotechnology, 1: 1000). All experiments were performed at least three times (i.e., three separate protein preparations) under the same conditions.

Li J., Li T., Li Z., Song Z, & Gong X. (2023). Nephroprotective mechanisms of Rhizoma Chuanxiong and Radix et Rhizoma Rhei against acute renal injury and renal fibrosis based on network pharmacology and experimental validation. Frontiers in Pharmacology, 14, 1154743.

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